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Functional architecture of RNA polymerase I

Title data

Kuhn, Claus-D. ; Geiger, Sebastian R. ; Baumli, Sonja ; Gartmann, Marco ; Gerber, Jochen ; Jennebach, Stefan ; Mielke, Thorsten ; Tschochner, Herbert ; Beckmann, Roland ; Cramer, Patrick:
Functional architecture of RNA polymerase I.
In: Cell. Vol. 131 (2007) Issue 7 . - pp. 1260-1272.
ISSN 0092-8674
DOI: https://doi.org/10.1016/j.cell.2007.10.051

Official URL: Volltext

Abstract in another language

Synthesis of ribosomal RNA (rRNA) by RNA polymerase (Pol) I is the first step in ribosome biogenesis and a regulatory switch in eukaryotic cell growth. Here we report the 12 A cryo-electron microscopic structure for the complete 14-subunit yeast Pol I, a homology model for the core enzyme, and the crystal structure of the subcomplex A14/43. In the resulting hybrid structure of Pol I, A14/43, the clamp, and the dock domain contribute to a unique surface interacting with promoter-specific initiation factors. The Pol I-specific subunits A49 and A34.5 form a heterodimer near the enzyme funnel that acts as a built-in elongation factor and is related to the Pol II-associated factor TFIIF. In contrast to Pol II, Pol I has a strong intrinsic 3'-RNA cleavage activity, which requires the C-terminal domain of subunit A12.2 and, apparently, enables ribosomal RNA proofreading and 3'-end trimming.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Binding Sites; Cryoelectron Microscopy; Crystallography, X-Ray; DNA Polymerase I/*chemistry/genetics/metabolism; Models, Molecular; Mutation; Peptide Elongation Factors/chemistry/metabolism; Peptide Initiation Factors/chemistry/metabolism; Promoter Regions, Genetic; Protein Conformation; Protein Interaction Domains and Motifs; Protein Interaction Mapping; Protein Structure, Tertiary; Protein Subunits; *RNA Processing, Post-Transcriptional; RNA, Ribosomal/genetics/*metabolism; Saccharomyces cerevisiae/*enzymology/genetics; Saccharomyces cerevisiae Proteins/*chemistry/genetics/metabolism; Structure-Activity Relationship; Transcription Factors, TFII/chemistry/metabolism; *Transcription, Genetic; Transcriptional Elongation Factors/chemistry/metabolism
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Profile Fields > Advanced Fields > Molecular Biosciences
Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Profile Fields
Profile Fields > Advanced Fields
Research Institutions
Research Institutions > Research Centres
Result of work at the UBT: No
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 10 Jan 2017 11:20
Last Modified: 10 Jan 2017 11:20
URI: https://eref.uni-bayreuth.de/id/eprint/35642